Evidence map›Paper›PMID 26195665›Full record

ArticleThe Journal of cell biology2015

The deubiquitinating enzyme complex BRISC is required for proper mitotic spindle assembly in mammalian cells.

Kaowen Yan, Li Li, Xiaojian Wang, Ruisha Hong, Ying Zhang, Hua Yang, Ming Lin, Sha Zhang, Qihua He, Duo Zheng and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
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  6. Article
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  8. Article
  9. Review
  10. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  11. ABRO1 arrests cardiomyocyte proliferation and myocardial repair by suppressing PSPH.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Regulation of oxidized LDL-induced inflammatory process through NLRP3 inflammasome activation by the deubiquitinating enzyme BRCC36.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2019
    Article
  20. Deubiquitinating Enzymes: A Critical Regulator of Mitosis.International journal of molecular sciences · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 1 country.

Kaowen YanDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China Institute of Systems Biomedicine, Beijing Key Laboratory of Tumor Systems Biology, Peking University, Beijing 100191, China.
Li LiDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
Xiaojian WangState Key Laboratory of Agrobiotechnology, College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
Ruisha HongDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China School of Medicine, Shenzhen University, Shenzhen, Guangdong 518060, China.
Ying ZhangDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
Hua YangDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
Ming LinDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
Sha ZhangDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
Qihua HeCenter of Medical and Health Analysis, Peking University, Beijing 100191, China.
Duo ZhengSchool of Medicine, Shenzhen University, Shenzhen, Guangdong 518060, China.
Jun TangState Key Laboratory of Agrobiotechnology, College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
Yuxin YinInstitute of Systems Biomedicine, Beijing Key Laboratory of Tumor Systems Biology, Peking University, Beijing 100191, China.
Genze ShaoDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing 100191, China Institute of Systems Biomedicine, Beijing Key Laboratory of Tumor Systems Biology, Peking University, Beijing 100191, China gzshao@bjmu.edu.cn lily@bjmu.edu.cn.
Peking University · CNChina Agricultural University · CNShenzhen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deubiquitinating enzymes (DUBs) negatively regulate protein ubiquitination and play an important role in diverse physiological processes, including mitotic division. The BRCC36 isopeptidase complex (BRISC) is a DUB that is specific for lysine 63-linked ubiquitin hydrolysis; however, its biological function remains largely undefined. Here, we identify a critical role for BRISC in the control of mitotic spindle assembly in cultured mammalian cells. BRISC is a microtubule (MT)-associated protein complex that predominantly localizes to the minus ends of K-fibers and spindle poles and directly binds to MTs; importantly, BRISC promotes the assembly of functional bipolar spindle by deubiquitinating the essential spindle assembly factor nuclear mitotic apparatus (NuMA). The deubiquitination of NuMA regulates its interaction with dynein and importin-β, which are required for its function in spindle assembly. Collectively, these results uncover BRISC as an important regulator of the mitotic spindle assembly and cell division, and have important implications for the development of anticancer drugs targeting BRISC.

Indexed as

UbiquitinationAdaptor Proteins, Signal TransducingAntigens, NuclearCell Cycle ProteinsDeubiquitinating EnzymesHEK293 CellsHeLa CellsHumansKinetochoresMembrane ProteinsMicrotubulesM Phase Cell Cycle CheckpointsMultienzyme ComplexesNuclear Matrix-Associated ProteinsProtein TransportSpindle ApparatusABRAXAS2 protein, humanAdaptor Proteins, Signal TransducingAntigens, NuclearBABAM1 protein, humanBRCC3 protein, humanCell Cycle ProteinsDeubiquitinating EnzymesMembrane ProteinsMultienzyme ComplexesNuclear Matrix-Associated ProteinsNUMA1 protein, humanUbiquitin-Specific Proteases

Identifiers

PMID26195665
PMCPMC4508884
OpenAlexW2168718892

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.